田邊　賢司    Department   Research Institutes and Facilities, Research Institutes and Facilities    Position   Associate Professor
Article types	Original article
Language	English
Peer review	Peer reviewed
Title	Filamin A-bound PEBP2beta/CBFbeta is retained in the cytoplasm and prevented from functioning as a partner of the Runx1 transcription factor.
Journal	Formal name：Molecular and cellular biology
Volume, Issue, Page	25,pp.1003-1012
Author and coauthor	Yoshida, Naomi Ogata, Takehiro Tanabe, Kenji Li, Songhua Nakazato, Megumi Kohu, Kazuyoshi Takafuta, Toshiro Shapiro, Sandor Ohta, Yasutaka Satake, Masanobu Watanabe, Toshio
Publication date	2005
Summary	The heterodimeric transcription factor PEBP2/CBF is composed of a DNA-binding subunit, called Runx1, and a non-DNA-binding subunit, called PEBP2beta/CBFbeta. The Runx1 protein is detected exclusively in the nuclei of most cells and tissues, whereas PEBP2beta is located in the cytoplasm. We addressed the mechanism by which PEBP2beta localizes to the cytoplasm and found that it is associated with filamin A, an actin-binding protein. Filamin A retains PEBP2beta in the cytoplasm, thereby hindering its engagement as a Runx1 partner. The interaction with filamin A is mediated by a region within PEBP2beta that includes amino acid residues 68 to 93. The deletion of this region or the repression of filamin A enables PEBP2beta to translocate to the nucleus. Based on these observations, we propose that PEBP2beta has two distinct domains, a newly defined regulatory domain that interacts with filamin A and the previously identified Runx1-binding domain.